Helminth parasites secrete extracellular vesicles (EVs) as a means of exporting effector molecules into the host microenvironment. Once released, the parasite-derived EVs are internalised by host immune cells and trigger a range of biological effects including modulation of host immunity. While the molecular cargo of EVs have been characterised in many parasites, little is known about the surface-exposed molecules that may effect ligand-receptor interactions with the target host cell surface that initiate vesicle docking and subsequent internalisation. Here we used a membrane-impermeable biotin reagent to capture proteins displayed on the outer membrane surface of adult F. hepatica EVs and mass spectrometry to identified the surface proteins.